ID R8WV51_9ENTR Unreviewed; 120 AA.
AC R8WV51;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dihydroneopterin triphosphate 2'-epimerase {ECO:0000256|ARBA:ARBA00044197};
DE EC=5.1.99.7 {ECO:0000256|ARBA:ARBA00044039};
DE AltName: Full=D-erythro-7,8-dihydroneopterin triphosphate epimerase {ECO:0000256|ARBA:ARBA00044306};
GN ORFNames=WC7_02993 {ECO:0000313|EMBL:EOQ48748.1};
OS Citrobacter sp. KTE151.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=1169322 {ECO:0000313|EMBL:EOQ48748.1, ECO:0000313|Proteomes:UP000014006};
RN [1] {ECO:0000313|EMBL:EOQ48748.1, ECO:0000313|Proteomes:UP000014006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE151 {ECO:0000313|EMBL:EOQ48748.1,
RC ECO:0000313|Proteomes:UP000014006};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE151.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin
CC 3'-triphosphate; Xref=Rhea:RHEA:28346, ChEBI:CHEBI:58462,
CC ChEBI:CHEBI:61186; EC=5.1.99.7;
CC Evidence={ECO:0000256|ARBA:ARBA00043806};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOQ48748.1}.
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DR EMBL; ASQK01000005; EOQ48748.1; -; Genomic_DNA.
DR RefSeq; WP_016153849.1; NZ_KB976064.1.
DR AlphaFoldDB; R8WV51; -.
DR GeneID; 66273612; -.
DR PATRIC; fig|1169322.3.peg.2989; -.
DR HOGENOM; CLU_112632_0_0_6; -.
DR Proteomes; UP000014006; Unassembled WGS sequence.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
DR CDD; cd00534; DHNA_DHNTPE; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR NCBIfam; TIGR00526; folB_dom; 1.
DR PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR PANTHER; PTHR42844:SF10; DIHYDRONEOPTERIN TRIPHOSPHATE 2'-EPIMERASE; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 4: Predicted;
FT DOMAIN 8..118
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 120 AA; 13997 MW; B17D79D8E72DC729 CRC64;
MSQPDAIIRI KNLRLRTFIG IKEEEILNRQ DIVINIAIHY PADKARTSED INDALNYRTI
TKSIIAHVEG NRFSLLEKLT QDVLDIAREH HWVTYAQVEI DKLHALRYAD SVSMTLSWQR
//